About: Built‐in RNA‐mediated chaperone (chaperna) for antigen folding tailored to immunized hosts

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About: Built‐in RNA‐mediated chaperone (chaperna) for antigen folding tailored to immunized hosts Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Built‐in RNA‐mediated chaperone (chaperna) for antigen folding tailored to immunized hosts
Creator	Kim, Young-Seok Kim, Jihoon Oh, Hana Kim, Yeon-Sook Cho, Nam-Hyuk Sung, Jemin Nam, Jae-Hwan Lee, Eun-Young Chae, Wonil Baik, \| Cheong, Yucheol Choi, Seongil Kang, \| Sang-Moo Lim, Jongkwan Seong, L
source	PMC
abstract	High‐quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA‐dependent chaperone, in which the target antigen is genetically fused with an RNA‐interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N‐terminal tRNA‐binding domain of lysyl‐tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the “self” RID tag remained nonimmunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS‐CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc‐mediated effector function was demonstrated, which could be harnessed for the design of next‐generation “universal” influenza vaccines. The nonimmunogenic built‐in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics, and designer vaccines.
has issue date	2020-05-02(xsd:dateTime)
bibo:doi	10.1002/bit.27355
has license	cc-by
sha1sum (hex)	75c09abecc85a8a31b51d47e67d0c7a7862f235c
schema:url	https://doi.org/10.1002/bit.27355
resource representing a document's title	Built‐in RNA‐mediated chaperone (chaperna) for antigen folding tailored to immunized hosts
has PubMed Central identifier	PMC7262357
schema:publication	Biotechnol Bioeng
resource representing a document's body	covid:75c09abecc85a8a31b51d47e67d0c7a7862f235c#body_text
is schema:about of	named entity 'selected' named entity 'availability' named entity 'bacterial' named entity 'domain' named entity 'antigen' covid:arg/75c09abecc85a8a31b51d47e67d0c7a7862f235c named entity 'host' named entity 'target' named entity 'soluble' named entity 'hosts' named entity 'antigens' named entity 'depends' named entity 'demonstrated' named entity 'fusion' named entity 'viral' named entity 'derived' named entity 'immunologically' named entity 'infection' named entity 'antigens' named entity 'hybridoma' named entity 'monoclonal antibodies' named entity 'antigen' named entity 'clones' named entity 'LysRS' named entity 'MERS-CoV' named entity 'binding domain' named entity 'tRNA synthetase' named entity 'High-quality' named entity 'N-terminal' named entity 'influenza hemagglutinin' named entity 'mAb' named entity 'RBD' named entity 'Eukaryotic' named entity 'HR2' named entity 'mAb' named entity '293T' named entity 'IAV' named entity 'radial immunodiffusion' named entity 'protein' named entity 'Victoria' named entity 'insoluble' named entity 'E. coli' named entity 'substrate' named entity 'polyclonal' named entity 'RNAs' named entity 'RNA' named entity 'tRNA' named entity 'antigen' named entity 'Middle East' named entity 'Hybridoma' named entity 'polyacrylamide gel electrophoresis' named entity 'precipitation' named entity '2-mercaptoethanol' named entity 'supernatant' named entity 'solubility' named entity 'mAb' named entity 'Middle East respiratory syndrome' named entity 'globular domains' named entity 'LysRS' named entity 'antigens' named entity 'skim milk' named entity 'fusion partners' named entity 'cell culture' named entity 'Kent' named entity 'solubility' named entity 'mAbs' named entity 'RNA-binding' named entity 'viruses' named entity 'Francin'

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